4ukd: Difference between revisions

Revision as of 13:53, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:4ukd.png

Template:STRUCTURE 4ukd

UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, UDP, BERYLLIUM FLUORIDEUMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, UDP, BERYLLIUM FLUORIDE

Template:ABSTRACT PUBMED 9280438

About this StructureAbout this Structure

4UKD is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

ReferenceReference

Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative., Schlichting I, Reinstein J, Biochemistry. 1997 Aug 5;36(31):9290-6. PMID:9280438

Page seeded by OCA on Thu Jul 3 13:53:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:4ukd.gif|left|200px]]
+{{Seed}}
+[[Image:4ukd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_4ukd|  PDB=4ukd  |  SCENE=  }}
-'''UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, UDP, BERYLLIUM FLUORIDE'''
+===UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, UDP, BERYLLIUM FLUORIDE===
-==Overview==
+<!--
-UMP/CMP kinase from Dictyostelium discoideum (UmpKdicty) catalyzes the specific transfer of the terminal phosphate of ATP to UMP or CMP. Crystal structures of UmpKdicty with substrates and the transition state analogs AlF3 or BeF2 that lock UmpKdicty in active conformations were solved. The positions of the catalytic Mg2+ and the highly conserved lysine of the P loop are virtually invariant in the different structures. In contrast, catalytic arginines move to stabilize charges that develop during this reaction. The location of the arginines indicates formation of negative charges during the reaction at the transferred phosphoryl group, but not at the phosphate bridging oxygen atoms. This is consistent with an associative phosphoryl transfer mechanism but not with a dissociative one.
+The line below this paragraph, {{ABSTRACT_PUBMED_9280438}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9280438 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9280438}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Transferase]]
 [[Category: Transition state analog complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:30:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:53:54 2008''